Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat.

Koelle, George B.; Massoulié, Jean; Eugène, Daniel; Melone, Mariarosa Anna Beatrice; Boulla, Geneviève

doi:10.1073/pnas.84.21.7749

Cited by 17 publications

(16 citation statements)

References 31 publications

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“…Total AcChoEase. When AcChoEase was not inhibited before culture, we obtained a pattern of molecular forms that closely resembled that observed with freshly excised normal cat SCG (9). The G4 form markedly predominated over the G1 and G2 forms, and there was an extremely small A12 peak ( Fig.…”

Section: Resultsmentioning

confidence: 70%

“…The protein concentration of extracts was determined with the method of Lowry et al (11) or of Bradford (12). The activities of lactate dehydrogenase (LDH) and enolase were determined as indicated previously (9). An aqueous extract of cat central nervous system, which was used in a few experiments, was prepared and dialyzed exactly as described previously (1,3) and was stored at -70°C.…”

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confidence: 99%

“…The gradients were centrifuged for 18 hr at 39,000 rpm in a Beckman SW 41 rotor at 4-50C. Approximately 42 fractions were collected and assayed by a modification of Ellman's method (10) as indicated previously (9). Astra 1397…”

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confidence: 99%

“…The SCGs were then homogenized in a high-salt and Triton X-100-containing extraction medium to solubilize AcChoEase. The molecular forms of the enzyme were analyzed by sedimentation in sucrose density gradients, as described previously (9). METHODS We cultured sections of cat SCG with a number of variations: the interval between preganglionic denervation and excision, omission of denervation, time in culture, and inclusion or omission of near-total inactivation of AcChoEase and BtChoEase before culture.…”

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Effects of glycyl-L-glutamine in vitro on the molecular forms of acetylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

Koelle¹,

Massoulié²,

Eugène³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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Normal and preganglionically denervated cat superior cervical ganglia were sectioned and cultured for 24 or 48 hr, with or without preliminary inactivation of acetylcholinesterase, and in the presence or absence of 10-5 M glycyl-L-glutamine. They were then homogenized, and the molecular forms of acetylcholinesterase were analyzed by sucrose gradient sedimentation. We observed an increased proportion of the globular monomeric G, form, and to a lesser extent of the dimeric G2 and tetrameric membranous G4 forms, of acetylcholinesterase in the glycyl-L-glutamine-treated compared with the control cultures. There was only a small increase in the total acetylcholinesterase activity and no significant variation in the activity of the metabolic enzyme lactate dehydrogenase. It therefore seems likely that glycyl-L-glutamine, or the endogenous neurotrophic factor, maintains acetylcholinesterase in the preganglionically denervated ganglia in vivo by specifically increasing the biosynthesis of the monomeric G, form, but not that of other proteins; these trophic factors do not seem to promote the polymerization of G, into the more complex G2 and G4 forms.Preganglionic denervation of the cat superior cervical ganglion (SCG) results within a few days in a marked decrease in its contents of acetylcholinesterase (AcChoEase, EC 3.1.1.7) and butyrylcholinesterase (BtChoEase, EC 3.1.1.8) (1, 2). In a recent series of experiments (1, 3-6) it was shown that the 24-hr intracarotid infusion of a dialyzed aqueous extract of cat brain, spinal cord, and sciatic nerves, or of glycyl-L-glutamine (Gly-Gln), or of some closely related compounds, opposes the decrease of both enzymes. Gly-Gln was tested after the demonstration by Haynes and Smith (7) that this compound increases the formation of the G4 (globular tetramer) and A12 (collagen-tailed, asymmetric dodecamer) forms of AcChoEase (8) in cultured preparations of embryonic rat and chicken skeletal muscle.In the present study we investigated the stage at which Gly-Gln, or the unidentified endogenous neurotrophic factor, enhances the production of AcChoEase in denervated ganglia. In an effort to study this effect in vitro, we first used whole desheathed rat SCG that had been preganglionically denervated one day previously. Results were suggestive, but equivocal, probably for the reasons given in the Discussion and, consequently, are not presented.In the experiments reported here, sections of normal or preganglionically denervated cat SCG were incubated in culture medium for 24 or 48 hr, with or without inactivation of their initial AcChoEase content, and with or without the addition of Gly-Gln or nervous tissue extract. The SCGs were then homogenized in a high-salt and Triton X-100-containing extraction medium to solubilize AcChoEase. The molecular forms of the enzyme were analyzed by sedimentation in sucrose density gradients, as described previously (9). METHODSWe cultured sections of cat SCG with a number of variations: the interval between preganglionic denervation and excision, ...

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Section: Resultsmentioning

confidence: 70%

mentioning

confidence: 99%

mentioning

confidence: 99%

mentioning

confidence: 99%

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Effects of glycyl-L-glutamine in vitro on the molecular forms of acetylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

Koelle¹,

Massoulié²,

Eugène³

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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“…A subset of these molecules may be targeted to the neuromuscular junction and other synapses. By using electron microscopic histochemical methods and biochemical techniques in conjunction with denervation studies, it has been possible to correlate the location of several AcChoEase molecular forms with specific regions of the neurons (24,25). These studies suggest that the monomeric AcChoEase molecules are localized within the neuronal perikarya whereas the multimeric forms are transported away from the perikarya and localized along the axonal plasma membrane and at sites of nerve contact on both the pre-and postsynaptic membranes.…”

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Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.

Rotundo

Gómez

Fernández‐Valle

et al. 1988

Proc. Natl. Acad. Sci. U.S.A.

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Postnatal development of acetylcholinesterase in, and cholinergic projections to, the cat superior colliculus

McHaffie

Beninato

Stein

et al. 1991

J of Comparative Neurology

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The postnatal development of cholinergic afferents to the superior colliculus in neonatal cats was studied by using acetylcholinesterase (AChE) histochemistry, choline acetyltransferase (ChAT) immunohistochemistry, and retrograde transport of horseradish peroxidase (HRP). In the adult cat, the pattern of AChE staining was laminar specific. AChE was distributed continuously in the stratum griseum superficiale (SGS) but was organized as patches in the stratum griseum intermediate (SGI). Diffuse AChE staining also was present in the stratum griseum profundum (SGP) and the dorsolateral periaqueductal gray (PAG). At birth, however, AChE staining was barely detectable in the SGS and, aside from a few isolated labeled neurons, was absent from the SGI, SGP, and PAG. By 7 days postnatal (dpn), staining in the SGS was more apparent but did not change appreciably in the deeper laminae. A substantial increase in AChE staining occurred in the SGS at 14 dpn (several days after eye opening), at which time patches in the SGI first became apparent. By 28 dpn, the complete laminar-specific adult AChE staining pattern was present, though the staining intensity did not reach the adult level until 56 dpn. A protracted maturation of both AChE staining and ChAT immunoreactivity also was observed in the sources of cholinergic afferents to the superior colliculus, which include the parabigeminal nucleus, and the pedunculopontine (PPN) and lateral dorsal tegmental (LDTN) nuclei. AChE and ChAT-immunoreactive staining in each nucleus was weak at birth but increased during the ensuing 2 weeks. At 21 dpn, however, ChAT immunoreactivity virtually disappeared in the parabigeminal nucleus and significantly decreased in PPN and LDTN. The ChAT immunoreactivity in these nuclei then gradually increased reaching maximum levels by 28 dpn. At 35 dpn, AChE staining showed a significant, though temporary (4 weeks), decrease in the parabigeminal nucleus, but not in the PPN and LDTN, that subsequently increased to the adult level of staining at 70 dpn. The absence of AChE in the SGI in neonatal animals was correlated, at least in part, with a paucity of neurons in the brainstem cholinergic cell groups labeled by retrograde transport of HRP from the superior colliculus. Injections of HRP into the superior colliculus retrogradely labeled many neurons in the parabigeminal nucleus, but few, if any, neurons in the PPN or LDTN at 1 dpn. Retrogradely labeled neurons also were observed in the substantia nigra pars reticulata, albeit fewer in neonates than in adults.(ABSTRACT TRUNCATED AT 400 WORDS)

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Distributions of molecular forms of acetylcholinesterase and butyrylcholinesterase in nervous tissue of the cat.

Cited by 17 publications

References 31 publications

Effects of glycyl-L-glutamine in vitro on the molecular forms of acetylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

Effects of glycyl-L-glutamine in vitro on the molecular forms of acetylcholinesterase in the preganglionically denervated superior cervical ganglion of the cat.

Allelic variants of acetylcholinesterase: genetic evidence that all acetylcholinesterase forms in avian nerves and muscles are encoded by a single gene.

Postnatal development of acetylcholinesterase in, and cholinergic projections to, the cat superior colliculus

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